2cqm

Solution structure of the mitochondrial ribosomal protein L17 isolog

Method: SOLUTION NMR Dmax: 65.2 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribosomal protein L17 isolog

Homo sapiens

UniProt Q9NRX2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–136 Fragment:Mitochondrial ribosomal protein L17 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.1mM 13C/15N-PROTEIN; 20mM d-Tris-HCl; 200mM NaCl; 1mM d-DTT; 0.02% NaN3 | 90% H2O/10% D2O Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

87 other PDB entries and 87 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9NRX2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–116; UniProt 28–136

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2cqm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2cqm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2cqm
Deposition date deposition_date2005-05-20
Structure title titleSolution structure of the mitochondrial ribosomal protein L17 isolog
Keywords keywords;alpha and beta (a+b), Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Translation ;; TRANSLATION
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.25
Radius of gyration Rg (electron density) rg_electron15.76
Forward intensity I(0) i01047300000.00
Molecular weight molecular_weight273040.0 kDa
Excluded volume excluded_volume341960 ų
Envelope volume envelope_volume46732 ų
Hydration-shell volume shell_volume19674 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg26.63
Envelope Rg envelope_rg21.21
Shape Rg shape_rg15.74
Total Rg total_rg16.03
Total atoms total_atoms38620
Residues n_residues2440
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax65.2
Rg (real space) rg_real16.35
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real1.0470e+09
I(0) uncertainty (real space) i0_real_error1.3670e+07
Rg (reciprocal space) rg_reciprocal16.34
I(0) (reciprocal space) i0_reciprocal1047000000.0000
Solution quality estimate total_estimate0.7495
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.5
Skewness Skewness skewness0.575
Kurtosis Kurtosis kurtosis0.233
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha622900.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.355; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.676; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2cqma1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.188 — Prokaryotic ribosomal protein L17
Superfamily Superfamily superfamilyd.188.1 — Prokaryotic ribosomal protein L17
Family Family familyd.188.1.1 — Prokaryotic ribosomal protein L17
Domain ID domain_idd2cqma2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2cqma3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2cqmA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1030 — 50s Ribosomal Protein L17; Chain: A,
Homologous superfamily homologous superfamily10 — Ribosomal protein L17

8. Citations (1)

9. Files and Curves (10)